GBGT1_MOUSE
ID GBGT1_MOUSE Reviewed; 347 AA.
AC Q8VI38; Q3KPA1; Q8CJF3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE EC=2.4.1.88 {ECO:0000250|UniProtKB:Q95158};
DE AltName: Full=Forssman glycolipid synthase;
GN Name=Gbgt1 {ECO:0000312|MGI:MGI:2449143}; Synonyms=Fgs;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14573676; DOI=10.1128/iai.71.11.6543-6552.2003;
RA Elliott S.P., Yu M., Xu H., Haslam D.B.;
RT "Forssman synthetase expression results in diminished shiga toxin
RT susceptibility: a role for glycolipids in determining host-microbe
RT interactions.";
RL Infect. Immun. 71:6543-6552(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Watanobe T., Shimizu M., Nakano M., Handa S., Yoshida M., Kushi Y.;
RT "Preferential expression of Forssman glycolipid in undifferentiated ES
RT cells and its chromosomal localization in mouse.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the formation of Forssman glycolipid via the
CC addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to
CC GalNAcb-1,3Gala-1,4Galb-1,4GlcCer (Gb4Cer) (PubMed:14573676). Forssman
CC glycolipid (also called Forssman antigen; FG) probably serves for
CC adherence of some pathogens (PubMed:14573676). Conversely, it
CC diminishes Shiga toxins susceptibility (PubMed:14573676).
CC {ECO:0000269|PubMed:14573676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb4Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = globoside Forssman (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:22164, ChEBI:CHEBI:15378, ChEBI:CHEBI:18056,
CC ChEBI:CHEBI:18259, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.88;
CC Evidence={ECO:0000250|UniProtKB:Q95158};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22165;
CC Evidence={ECO:0000250|UniProtKB:Q95158};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb4Cer + UDP-N-acetyl-alpha-D-galactosamine =
CC globoside IV3GalNAc-Gb4Cer + H(+) + UDP; Xref=Rhea:RHEA:56568,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:88167, ChEBI:CHEBI:90400;
CC Evidence={ECO:0000269|PubMed:14573676};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56569;
CC Evidence={ECO:0000305|PubMed:14573676};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- DOMAIN: The conserved DXD motif is involved in cofactor binding. The
CC manganese ion interacts with the beta-phosphate group of UDP and may
CC also have a role in catalysis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Globoside
CC alpha-1,3-N-acetylgalactosaminyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=gt_mou_504";
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DR EMBL; AF292399; AAL37034.1; -; mRNA.
DR EMBL; AB084789; BAC23060.2; -; mRNA.
DR EMBL; AL772249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106831; AAI06832.1; -; mRNA.
DR CCDS; CCDS15839.1; -.
DR RefSeq; NP_631936.2; NM_139197.2.
DR RefSeq; XP_006497981.1; XM_006497918.2.
DR AlphaFoldDB; Q8VI38; -.
DR SMR; Q8VI38; -.
DR STRING; 10090.ENSMUSP00000127071; -.
DR SwissLipids; SLP:000001914; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; Q8VI38; 1 site.
DR PhosphoSitePlus; Q8VI38; -.
DR MaxQB; Q8VI38; -.
DR PaxDb; Q8VI38; -.
DR PRIDE; Q8VI38; -.
DR ProteomicsDB; 266779; -.
DR Antibodypedia; 63936; 56 antibodies from 16 providers.
DR DNASU; 227671; -.
DR Ensembl; ENSMUST00000028172; ENSMUSP00000028172; ENSMUSG00000026829.
DR Ensembl; ENSMUST00000163121; ENSMUSP00000127071; ENSMUSG00000026829.
DR GeneID; 227671; -.
DR KEGG; mmu:227671; -.
DR UCSC; uc008iyl.2; mouse.
DR CTD; 26301; -.
DR MGI; MGI:2449143; Gbgt1.
DR VEuPathDB; HostDB:ENSMUSG00000026829; -.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR HOGENOM; CLU_062445_0_1_1; -.
DR InParanoid; Q8VI38; -.
DR OMA; IHPGYFT; -.
DR OrthoDB; 1204439at2759; -.
DR PhylomeDB; Q8VI38; -.
DR TreeFam; TF330991; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 227671; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Gbgt1; mouse.
DR PRO; PR:Q8VI38; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VI38; protein.
DR Bgee; ENSMUSG00000026829; Expressed in hindlimb stylopod muscle and 56 other tissues.
DR Genevisible; Q8VI38; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0047277; F:globoside alpha-N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0001575; P:globoside metabolic process; ISS:UniProtKB.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Globoside alpha-1,3-N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000157296"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 116..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 228..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 337
FT /note="S -> P (in Ref. 1; AAL37034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 40502 MW; 69C7E141334A5F44 CRC64;
MTRPRLAQGL AFFLLGGTGL WVLWKFIKDW LLVSYIPYYL PCPEFFNMKL PFRKEKPLQP
VTQLQYPQPK LLEHGPTELL TLTPWLAPIV SEGTFDPELL KSMYQPLNLT IGVTVFAVGK
YTCFIQRFLE SAEEFFMRGY QVHYYLFTHD PTAVPRVPLG PGRLLSIIPI QGYSRWEEIS
MRRMETINKH IAKRAHKEVD YLFCVDVDMV FRNPWGPETL GDLVAAIHPG YFAVPRRKFP
YERRQVSSAF VADNEGDFYY GGALFGGRVA RVYEFTRACH MAILADKANS IMAAWQEESH
LNRHFIWHKP SKVLSPEYLW DERKPRPRSL KMIRFSSVKK NANWLRT
